Research workbench
Structure of mutant (E165H) of the hsdr subunit of the ECOR124I restriction enzyme in complex with ATP
Analyse Structure of mutant (E165H) of the hsdr subunit of the ECOR124I restriction… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XJX
- Type
- protein
- Length
- 1,724 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hsdr
- UniProt
- Q304R3
- Ligands
- ATP, MG
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hsdr | protein | 861 | 42% helix, 15% strand | Q304R3 |
| B | Hsdr | protein | 863 | 44% helix, 14% strand | Q304R3 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 551 | 0.84 | 0.89 | 65 | MG, ATP |
| 2 | 747 | 0.82 | 0.85 | 82 | MG, ATP |
| 3 | 1173 | 0.78 | 0.80 | 127 | empty |
| 4 | 730 | 0.74 | 0.80 | 57 | empty |
| 5 | 698 | 0.74 | 0.80 | 66 | empty |
Interfaces
1 interface between chains.
- A–B · 826 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 4XJX · Structure of mutant (E165H) of the hsdr subunit of the ECOR124I restriction enzyme in… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q304R3
- Elsewhere: RCSB PDB 4XJX · PDBe 4XJX · UniProt Q304R3
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